Small angle neutron scattering for the study of solubilised membrane proteins

  • Cécile Breyton
  • Frank Gabel
  • Mathilde Lethier
  • Ali Flayhan
  • Grégory Durand
  • Jean-Michel Jault
  • Céline Juillan-Binard
  • Lionel Imbert
  • Martine Moulin
  • Stéphanie Ravaud
  • Michael Härtlein
  • Christine Ebel
Regular Article

DOI: 10.1140/epje/i2013-13071-6

Cite this article as:
Breyton, C., Gabel, F., Lethier, M. et al. Eur. Phys. J. E (2013) 36: 71. doi:10.1140/epje/i2013-13071-6
Part of the following topical collections:
  1. Neutron Biological Physics

Abstract

Small angle neutron scattering (SANS) is a powerful technique for investigating association states and conformational changes of biological macromolecules in solution. SANS is of particular interest for the study of the multi-component systems, as membrane protein complexes, for which in vitro characterisation and structure determination are often difficult. This article details the important physical properties of surfactants in view of small angle neutron scattering studies and the interest to deuterate membrane proteins for contrast variation studies. We present strategies for the production of deuterated membrane proteins and methods for quality control. We then review some studies on membrane proteins, and focus on the strategies to overcome the intrinsic difficulty to eliminate homogeneously the detergent or surfactant signal for solubilised membrane proteins, or that of lipids for membrane proteins inserted in liposomes.

Graphical abstract

Keywords

Topical issue: Neutron Biological Physics 

Copyright information

© EDP Sciences, SIF, Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  • Cécile Breyton
    • 1
    • 2
    • 3
  • Frank Gabel
    • 1
    • 2
    • 3
  • Mathilde Lethier
    • 1
    • 2
    • 3
  • Ali Flayhan
    • 1
    • 2
    • 3
  • Grégory Durand
    • 4
    • 5
  • Jean-Michel Jault
    • 1
    • 2
    • 3
  • Céline Juillan-Binard
    • 1
    • 2
    • 3
  • Lionel Imbert
    • 1
    • 2
    • 3
  • Martine Moulin
    • 6
    • 7
  • Stéphanie Ravaud
    • 1
    • 2
    • 3
  • Michael Härtlein
    • 6
    • 7
  • Christine Ebel
    • 1
    • 2
    • 3
  1. 1.Institut de Biologie Structurale (IBS)Univ. Grenoble AlpesGrenobleFrance
  2. 2.CEA, DSV, IBSGrenobleFrance
  3. 3.CNRS, IBSGrenobleFrance
  4. 4.Equipe Chimie Bioorganique et Systèmes AmphiphilesUniversité d’Avignon et des Pays de VaucluseAvignonFrance
  5. 5.Institut des Biomolécules Max MousseronUMR 5247 CNRS-Universités Montpellier 1 & 2MontpellierFrance
  6. 6.Institute Max Von Laue Paul LangevinGrenoble 9France
  7. 7.Partnership for Structural BiologyILL EMBL Deuteration LabGrenoble 9France

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